BASE-STEP: A transportable antiproton reservoir for fundamental interaction studies

Smorra, C.; Abbass, F.; Schweitzer, D.; Bohman, M.; Devine, J. D.; Dutheil, Y.; Hobl, A.; Arndt, B.; Bauer, B. B.; Devlin, J. A.; Erlewein, S.; Fleck, M.; Jäger, J. I.; Latacz, B. M.; Micke, P.; Schiffelholz, M.; Umbrazunas, G.; Wiesinger, M.; Will, C.; Wursten, E.; Yildiz, H.; Blaum, K.; Matsuda, Y.; Mooser, A.; Ospelkaus, C.; Quint, W.; Soter, A.; Walz, J.; Yamazaki, Y.; Ulmer, S.

doi:10.1063/5.0155492

Cited by 2 publications

References 88 publications

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Ultra-thin polymer foil cryogenic window for antiproton deceleration and storage

Latacz,

Arndt,

Devlin

et al. 2023

Review of Scientific Instruments

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We present the design and characterization of a cryogenic window based on an ultra-thin aluminized biaxially oriented polyethylene terephthalate foil at T < 10 K, which can withstand a pressure difference larger than 1 bar at a leak rate <1×10−9 mbar l/s. Its thickness of ∼1.7 μm makes it transparent to various types of particles over a broad energy range. To optimize the transfer of 100 keV antiprotons through the window, we tested the degrading properties of different aluminum coated polymer foils of thicknesses between 900 and 2160 nm, concluding that 1760 nm foil decelerates antiprotons to an average energy of 5 keV. We have also explicitly studied the permeation as a function of coating thickness and temperature and have performed extensive thermal and mechanical endurance and stress tests. Our final design integrated into the experiment has an effective open surface consisting of seven holes with a diameter of 1 mm and will transmit up to 2.5% of the injected 100 keV antiproton beam delivered by the Antiproton Decelerator and Extra Low ENergy Antiproton ring facility of CERN.

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Ultra-thin polymer foil cryogenic window for antiproton deceleration and storage

Latacz,

Arndt,

Devlin

et al. 2023

Review of Scientific Instruments

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Alzheimer’s Disease: Diagnosis and Cure

Rai

2024

The Brain: A Systems Neuroscience Perspective

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Causative agents of Alzheimer’s disease are 1) amyloid β foldings, 2) neurofibrillary tangles, and 3) reactive gliosis. Interaction of Aβ with the prion protein within neurons has recently been suggested to be the basis for drug discovery. Prion protein is a membrane protein found on cell surfaces of diverse types [1]. The accumulation of misfolded and unfolded proteins (UP) generates stress in the endoplasmic reticulum. This stress worsens the health of the regular function of neuronal cells. The role of unfolded protein response in T cell development and function has also been acknowledged [2]. The induction of Femto particles (Fps) is proposed inside G protein-coupled receptors at an appropriate point in time to monitor the accumulation of unfolded proteins and to control the misfolding of amyloid β. These new particles of 10-15m are proposed to be produced in neurons of the bloodbrain barrier (BBB). Protons released by hemoglobin can be glued to their antiparticle, i.e., antiproton, in the conformational space of partially folded amyloid β polypeptides. Portable Penning antiproton traps are now available at CERN. Gluing of protons and antiprotons to form a femto particle is mediated by dopamine, a neurotransmitter in the excitatory synapses.Intraneuronal oxygen homeostasis also contributes to the control of the progression of the disease. Quantum entanglement between two fps (cf. Fig. 8), one in the neurons of the neurovascular system (NVU) and the other in cerebrospinal fluid (CSF), may be used to assess the efficiency of the process in a patient with AD. Our approach to the discovery of a drug for AD is based on monitoring and controlling the misfolding of amyloid β and the initiation of folding of unfolded proteins by the intervention of femto particles.

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BASE-STEP: A transportable antiproton reservoir for fundamental interaction studies

Cited by 2 publications

References 88 publications

Ultra-thin polymer foil cryogenic window for antiproton deceleration and storage

Ultra-thin polymer foil cryogenic window for antiproton deceleration and storage

Alzheimer’s Disease: Diagnosis and Cure

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